Abstract
We assessed the fibrillogenic properties of synthetic peptides corresponding to residues 13–26 of β/A4 amyloid, containing either the normal sequence (β13–26) or the mutations Glu22 to Gln (β13–26Q22) and Ala21 to Gly (β13–26G21). The kinetics of aggregation were monitored at 37°C and pH 7.4 by measuring the amount of peptide remaining in solution, using reverse-phase high performance liquid chromatography. Negative stain electron microscopy revealed that all of the peptides formed fibrils. However, β13–26Q22 showed greatly accelerated fibril formation compared to the other two. The results suggest that the Q22 mutation confers increased amyloidogenic properties on the β/A4 peptide, whereas the G21 mutation acts by a different pathogenic mechanism.
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